| IED ID | IndEnz0002016565 |
| Enzyme Type ID | protease016565 |
| Protein Name |
Probable cytosol aminopeptidase EC 3.4.11.1 Leucine aminopeptidase LAP EC 3.4.11.10 Leucyl aminopeptidase |
| Gene Name | pepA Bd3755 |
| Organism | Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Oligoflexia Bdellovibrionales Bdellovibrionaceae Bdellovibrio Bdellovibrio bacteriovorus Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100) |
| Enzyme Sequence | MAFNLLNKDIDTLTCPALVVFSKSSSQKDKLAKVTHSEIHKALLPSLEEKTISGKHQETVVFREFSFKGFRHVIVVGLGKENEITHESVRQSMASAYEAIKALNVTEAAVHFDGITAGKKDAADFAKATAEGLILTSYVFNELMSGKKETKEINVHVVSKMGNDKAVKAAFNEGAILGSVVNFSRRLGDLPGNLMTPTILADSAVEGAKGIANLKVTVWDKARIKKEKMGGLLGVSNGSDQEPRFIIMEYKGAAASKKPVCFVGKGLTFDCGGISIKPGAGMEEMKYDMCGGANVIGTLLAIAKLKLKVNAVGLVASTENLINGSATKPGDVHTARNGKTFEVNNTDAEGRLILADALSYATELQPQMIVDAATLTGAMVIALGNTHTGYFTRNSALKTKVEKAAAESGEWVWNMPLTDFHVKDMKGTYADLSNISSGKGAGSATAAAFLEQFVGEGIPWAHFDIAGTGWAVGNRLPYCPKKGASGAMIRTFVEIAKQYT |
| Enzyme Length | 500 |
| Uniprot Accession Number | Q6MH10 |
| Absorption | |
| Active Site | ACT_SITE 277; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 351; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; |
| DNA Binding | |
| EC Number | 3.4.11.1; 3.4.11.10 |
| Enzyme Function | FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (7) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,262 |
| Kinetics | |
| Metal Binding | METAL 265; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 270; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 270; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 288; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 347; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 349; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 349; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181 |
| Rhea ID | |
| Cross Reference Brenda |